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Conserved domains on  [gi|1907123900|ref|XP_036016423|]
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A disintegrin and metalloproteinase with thrombospondin motifs 10 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-205 7.08e-102

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


:

Pssm-ID: 239801  Cd Length: 207  Bit Score: 314.18  E-value: 7.08e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900   1 MMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQKSIVSHSGhgn 80
Cdd:cd04273    12 KMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKKLNPPND--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  81 aipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSINEDIGLATAFTIAHEIGHTFGMNHDGVGNGC 160
Cdd:cd04273    89 ----SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSC 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907123900 161 GARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 205
Cdd:cd04273   164 GPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 458-569 1.32e-29

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


:

Pssm-ID: 461796  Cd Length: 115  Bit Score: 113.44  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900 458 TIEGVFSPAlPGTGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFHLRQGPDQA 536
Cdd:pfam05986   1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907123900 537 QSLEALGPINASLIIMVLAQ---AELPALHYRFNAP 569
Cdd:pfam05986  80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 220-288 1.31e-15

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 71.99  E-value: 1.31e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907123900 220 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 288
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 358-456 3.23e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 63.96  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900 358 DFREMQCSEFDSVPFR-----GKFYTWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 424
Cdd:pfam19236   4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907123900 425 SGECKHVGCDRVLGSDLREDKCRVCGGDGSAC 456
Cdd:pfam19236  84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 699-753 3.77e-12

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 61.70  E-value: 3.77e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907123900 699 WATLDWSECTPSCGPGLRHRVVLCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRC 753
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 639-695 2.32e-11

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 59.39  E-value: 2.32e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907123900 639 WVVGNWSRCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACQGPMC 695
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 580-635 1.32e-10

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.46  E-value: 1.32e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907123900 580 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSSAVAPHYCSGHSKlPKRQRACNTEPC 635
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKK-PPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 758-807 9.33e-09

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 52.07  E-value: 9.33e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907123900 758 WVTSEWGECSTQCGLGQQQRTVRCT---SHTGQPSRECTEALRPSTMQQCEAK 807
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 821-853 9.24e-07

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


:

Pssm-ID: 462560  Cd Length: 31  Bit Score: 45.60  E-value: 9.24e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907123900 821 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTCQ 853
Cdd:pfam08686   1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 301-353 1.14e-04

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 40.65  E-value: 1.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907123900  301 WGPWTPWGDCSRSCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTNDCP 353
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-205 7.08e-102

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 314.18  E-value: 7.08e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900   1 MMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQKSIVSHSGhgn 80
Cdd:cd04273    12 KMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKKLNPPND--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  81 aipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSINEDIGLATAFTIAHEIGHTFGMNHDGVGNGC 160
Cdd:cd04273    89 ----SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSC 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907123900 161 GARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 205
Cdd:cd04273   164 GPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 458-569 1.32e-29

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 113.44  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900 458 TIEGVFSPAlPGTGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFHLRQGPDQA 536
Cdd:pfam05986   1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907123900 537 QSLEALGPINASLIIMVLAQ---AELPALHYRFNAP 569
Cdd:pfam05986  80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 11-208 5.14e-26

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 106.23  E-value: 5.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  11 VEQYVLAIMNIVAKLFQDSslgNIVNILVTRLILLTEDQptLEITHHAGKSLDSFCKWQKSIVSHSghgnaipengvANH 90
Cdd:pfam01421  24 VRQRVFQVVNLVNSIYKEL---NIRVVLVGLEIWTDEDK--IDVSGDANDTLRNFLKWRQEYLKKR-----------KPH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  91 DTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSINEDIG---LATAFTIAHEIGHTFGMNHDGVGNGCGARGQDP 167
Cdd:pfam01421  88 DVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAHELGHNLGMQHDDFNGGCKCPPGGG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907123900 168 AkLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 208
Cdd:pfam01421 162 C-IMNPSAG-SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 220-288 1.31e-15

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 71.99  E-value: 1.31e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907123900 220 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 288
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 358-456 3.23e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 63.96  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900 358 DFREMQCSEFDSVPFR-----GKFYTWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 424
Cdd:pfam19236   4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907123900 425 SGECKHVGCDRVLGSDLREDKCRVCGGDGSAC 456
Cdd:pfam19236  84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 699-753 3.77e-12

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 61.70  E-value: 3.77e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907123900 699 WATLDWSECTPSCGPGLRHRVVLCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRC 753
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 639-695 2.32e-11

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 59.39  E-value: 2.32e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907123900 639 WVVGNWSRCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACQGPMC 695
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 580-635 1.32e-10

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.46  E-value: 1.32e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907123900 580 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSSAVAPHYCSGHSKlPKRQRACNTEPC 635
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKK-PPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 758-807 9.33e-09

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 52.07  E-value: 9.33e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907123900 758 WVTSEWGECSTQCGLGQQQRTVRCT---SHTGQPSRECTEALRPSTMQQCEAK 807
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 821-853 9.24e-07

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 462560  Cd Length: 31  Bit Score: 45.60  E-value: 9.24e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907123900 821 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTCQ 853
Cdd:pfam08686   1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 621-756 4.75e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 46.01  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900 621 SKLPKRQRACNTEPCPPDWVVGNWSR-----CSRSCDAGVRSRSVvCQRRVSAAEEKAlDDSACPQPRPpvleacQGPMC 695
Cdd:PHA02682   27 TKCPQATIPAPAAPCPPDADVDPLDKysvkeAGRYYQSRLKANSA-CMQRPSGQSPLA-PSPACAAPAP------ACPAC 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907123900 696 PPewATLDWSECTPSCGPGlrhrvvlCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRCPPA 756
Cdd:PHA02682   99 AP--AAPAPAVTCPAPAPA-------CPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPA 150
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 301-353 1.14e-04

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 40.65  E-value: 1.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907123900  301 WGPWTPWGDCSRSCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTNDCP 353
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 580-636 2.88e-04

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.49  E-value: 2.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907123900  580 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSsaVAPHYCSGHSklpKRQRACNTEPCP 636
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ--NGGGPCTGED---VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 758-805 3.44e-04

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.11  E-value: 3.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907123900  758 WVTSEWGECSTQCGLGQQQRTVRCTSHTGQ-PSRECTEAL---RPSTMQQCE 805
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQnGGGPCTGEDvetRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-205 7.08e-102

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 314.18  E-value: 7.08e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900   1 MMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQKSIVSHSGhgn 80
Cdd:cd04273    12 KMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKKLNPPND--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  81 aipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSINEDIGLATAFTIAHEIGHTFGMNHDGVGNGC 160
Cdd:cd04273    89 ----SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSC 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907123900 161 GARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 205
Cdd:cd04273   164 GPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 14-197 2.88e-34

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 129.85  E-value: 2.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  14 YVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQKSivshsghgnaipenGVANHDTA 93
Cdd:cd04267    27 YITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWRAE--------------GPIRHDNA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  94 VLITRYDIciyknKPCGTLGLAPVGGMCERERSCSINEDIGLA--TAFTIAHEIGHTFGMNHDGVGNGCGARGQDPAKLM 171
Cdd:cd04267    93 VLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTllTALTMAHELGHNLGAEHDGGDELAFECDGGGNYIM 167

                         170       180
                  ....*....|....*....|....*.
gi 1907123900 172 AAHITmKTNPFVWSSCSRDYITSFLD 197
Cdd:cd04267   168 APVDS-GLNSYRFSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 11-206 6.07e-30

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 117.33  E-value: 6.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  11 VEQYVLAIMNIVAKLFQDSslgNIvNILVTRLILLTEDQPtLEITHHAGKSLDSFCKWQKSIVSHSghgnaIPengvanH 90
Cdd:cd04269    24 VRQRVIEIVNIVDSIYRPL---NI-RVVLVGLEIWTDKDK-ISVSGDAGETLNRFLDWKRSNLLPR-----KP------H 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  91 DTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSINEDIG---LATAFTIAHEIGHTFGMNHDGVGNGCGARGQdp 167
Cdd:cd04269    88 DNAQLLT------GRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDDGGCTCGRSTC-- 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907123900 168 akLMAAHITmkTNPFVWSSCSRDYITSFLDSGLGLCLNN 206
Cdd:cd04269   160 --IMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 458-569 1.32e-29

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 113.44  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900 458 TIEGVFSPAlPGTGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFHLRQGPDQA 536
Cdd:pfam05986   1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907123900 537 QSLEALGPINASLIIMVLAQ---AELPALHYRFNAP 569
Cdd:pfam05986  80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 11-208 5.14e-26

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 106.23  E-value: 5.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  11 VEQYVLAIMNIVAKLFQDSslgNIVNILVTRLILLTEDQptLEITHHAGKSLDSFCKWQKSIVSHSghgnaipengvANH 90
Cdd:pfam01421  24 VRQRVFQVVNLVNSIYKEL---NIRVVLVGLEIWTDEDK--IDVSGDANDTLRNFLKWRQEYLKKR-----------KPH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  91 DTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSINEDIG---LATAFTIAHEIGHTFGMNHDGVGNGCGARGQDP 167
Cdd:pfam01421  88 DVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAHELGHNLGMQHDDFNGGCKCPPGGG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907123900 168 AkLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 208
Cdd:pfam01421 162 C-IMNPSAG-SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 220-288 1.31e-15

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 71.99  E-value: 1.31e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907123900 220 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 288
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 86-196 6.41e-13

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 67.55  E-value: 6.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  86 GVANHDTAVLITRYDiciyknKPCGTLGLAPVGGMCERERSCSINED---IGLATAFTIAHEIGHTFGMNHDGVGNGC-- 160
Cdd:cd00203    48 EIDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDnqsGTKEGAQTIAHELGHALGFYHDHDRKDRdd 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907123900 161 --------GARGQDPAKLMAAHIT--MKTNPFVWSSCSRDYITSFL 196
Cdd:cd00203   122 yptiddtlNAEDDDYYSVMSYTKGsfSDGQRKDFSQCDIDQINKLY 167
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 358-456 3.23e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 63.96  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900 358 DFREMQCSEFDSVPFR-----GKFYTWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 424
Cdd:pfam19236   4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907123900 425 SGECKHVGCDRVLGSDLREDKCRVCGGDGSAC 456
Cdd:pfam19236  84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 699-753 3.77e-12

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 61.70  E-value: 3.77e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907123900 699 WATLDWSECTPSCGPGLRHRVVLCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRC 753
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 89-204 1.28e-11

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800  Cd Length: 220  Bit Score: 65.07  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  89 NHDTAVLITRYDICIYKNKPC--GTLGLAPVGGMCErERSCSINEDigLATAF----TIAHEIGHTFGMNHDG---VGNG 159
Cdd:cd04272    94 NPDVVFLVTGLDMSTYSGGSLqtGTGGYAYVGGACT-ENRVAMGED--TPGSYygvyTMTHELAHLLGAPHDGsppPSWV 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907123900 160 CGARG--QDPAK---LMaAHITMKTNPFVWSSCSRDYITSFLDSGLGLCL 204
Cdd:cd04272   171 KGHPGslDCPWDdgyIM-SYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 639-695 2.32e-11

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 59.39  E-value: 2.32e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907123900 639 WVVGNWSRCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACQGPMC 695
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 580-635 1.32e-10

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.46  E-value: 1.32e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907123900 580 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSSAVAPHYCSGHSKlPKRQRACNTEPC 635
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKK-PPETQSCNLKPC 55
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 110-196 3.16e-09

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 372637  Cd Length: 193  Bit Score: 57.64  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900 110 GTLGLAPVGGMCERERSCsINEDIGLATAFT-------------IAHEIGHTFGMNHDGVG--------NGCGARGQDPA 168
Cdd:pfam13574  85 GELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGsqyassgcERNAATSVCSA 163

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907123900 169 K---LMAAhiTMKTNPFVWSSCSRDYITSFL 196
Cdd:pfam13574 164 NgsfIMNP--ASKSNNDLFSPCSISLICDVL 192
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
3-154 7.10e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 56.27  E-value: 7.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900   3 VAYHGRRDVEQYVLAIMNIVAKLFQDSSlgNIvNILVTRLILLTEDQPTleiTHHAGKSLDSFCKWQKSIVSHSghgnai 82
Cdd:pfam13688  16 VAAFGGDAAQANIINMVNTASNVYERDF--NI-SLGLVNLTISDSTCPY---TPPACSTGDSSDRLSEFQDFSA------ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  83 pENGVANHDTAVLITrydiciykNKPCGTLGLAPVGGMCERERSCSINEDIGLA--------TAFTIAHEIGHTFGMNHD 154
Cdd:pfam13688  84 -WRGTQNDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIGHNFGAVHD 154
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 758-807 9.33e-09

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 52.07  E-value: 9.33e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907123900 758 WVTSEWGECSTQCGLGQQQRTVRCT---SHTGQPSRECTEALRPSTMQQCEAK 807
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 14-154 1.45e-08

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 53.53  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  14 YVLAIMNIVAKLFQ-DSSLG-NIVNILVTRLilltEDQPTLEIThhAGKSLDSFckwQKSIVSHSGHGNAipengvanhD 91
Cdd:pfam13582   2 RIVSLVNRANTIYErDLGIRlQLAAIIITTS----ADTPYTSSD--ALEILDEL---QEVNDTRIGQYGY---------D 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907123900  92 TAVLITRYDiciyknkPCGTLGLAPVGGMCERERSCSINEDI---GLATAFTIAHEIGHTFGMNHD 154
Cdd:pfam13582  64 LGHLFTGRD-------GGGGGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 821-853 9.24e-07

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 462560  Cd Length: 31  Bit Score: 45.60  E-value: 9.24e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907123900 821 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTCQ 853
Cdd:pfam08686   1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 110-203 1.53e-05

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 47.37  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900 110 GTLGLAPV--------GGMCERE------RSCSINedIGLATAF-------------TIAHEIGHTFGMNHDGVGNGCGA 162
Cdd:cd04270   115 GTLGLAYVgsprdnsaGGICEKAyyysngKKKYLN--TGLTTTVnygkrvptkesdlVTAHELGHNFGSPHDPDIAECAP 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907123900 163 RGQDPAK-LMAAHITM--KTNPFVWSSCSRDYITSFLDSGLGLC 203
Cdd:cd04270   193 GESQGGNyIMYARATSgdKENNKKFSPCSKKSISKVLEVKSNSC 236
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 86-192 2.54e-05

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 404471  Cd Length: 203  Bit Score: 46.07  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900  86 GVANHDTAVLITRYdiciykNKPCGTLGLAPVGGMCERERScsiNEDIGLATAFT-----IAHEIGHTFGMNHDGVGNGC 160
Cdd:pfam13583  88 DSLNYDLAYLTLMT------GPSGQNVGVAWVGALCSSARQ---NAKASGVARSRdewdiFAHEIGHTFGAVHDCSSQGE 158

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907123900 161 GARGQ-DPAK---LMA-AHITMKTNpfvWSSCSRDYI 192
Cdd:pfam13583 159 GLSSStEDGSgqtIMSyASTASQTA---FSPCTIRNI 192
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 621-756 4.75e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 46.01  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123900 621 SKLPKRQRACNTEPCPPDWVVGNWSR-----CSRSCDAGVRSRSVvCQRRVSAAEEKAlDDSACPQPRPpvleacQGPMC 695
Cdd:PHA02682   27 TKCPQATIPAPAAPCPPDADVDPLDKysvkeAGRYYQSRLKANSA-CMQRPSGQSPLA-PSPACAAPAP------ACPAC 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907123900 696 PPewATLDWSECTPSCGPGlrhrvvlCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRCPPA 756
Cdd:PHA02682   99 AP--AAPAPAVTCPAPAPA-------CPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPA 150
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 301-353 1.14e-04

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 40.65  E-value: 1.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907123900  301 WGPWTPWGDCSRSCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTNDCP 353
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 580-636 2.88e-04

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.49  E-value: 2.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907123900  580 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSsaVAPHYCSGHSklpKRQRACNTEPCP 636
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ--NGGGPCTGED---VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 758-805 3.44e-04

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.11  E-value: 3.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907123900  758 WVTSEWGECSTQCGLGQQQRTVRCTSHTGQ-PSRECTEAL---RPSTMQQCE 805
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQnGGGPCTGEDvetRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
759-804 8.12e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.09  E-value: 8.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907123900 759 VTSEWGECSTQCGLGQQQRTVRC--TSHTGQPSRECTEALRPSTMQQC 804
Cdd:pfam00090   2 PWSPWSPCSVTCGKGIQVRQRTCksPFPGGEPCTGDDIETQACKMDKC 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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